Mapping the road to recovery: The ClpB/Hsp104 molecular chaperone

被引：33

作者：

Hodson, Skye ^{[1
]}

Marshall, Jacqueline J. T. ^{[1
]}

Burston, Steven G. ^{[1
]}

机构：

[1] Univ Bristol, Sch Biochem, Bristol BS8 1TD, Avon, England

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2012年 / 179卷 / 02期

基金：

英国生物技术与生命科学研究理事会;

关键词：

AAA plus -ATPase; Molecular chaperone; Hsp100; ClpB; Hsp104; Allostery; SACCHAROMYCES-CEREVISIAE HSP104; NUCLEOTIDE-BINDING DOMAINS; ESCHERICHIA-COLI PROTEINS; TERMINAL ATPASE DOMAIN; AAA PLUS PROTEIN; HEAT-SHOCK; THERMUS-THERMOPHILUS; AGGREGATED PROTEINS; CLPB CHAPERONE; SUBUNIT INTERACTIONS;

D O I：

10.1016/j.jsb.2012.05.015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The AAA.-ATPases are a family of molecular motors which have been seconded into a plethora of cellular tasks. One subset, the Hsp100 molecular chaperones, are general protein remodellers that help to maintain the integrity of the cellular proteome by means of protein destruction or resurrection. In this review we focus on one family of Hsp100s, the homologous ClpB and Hsp104 molecular chaperones that convey thermotolerance by resolubilising and rescuing proteins from aggregates. We explore how the nucleotide binding and hydrolysis properties at the twelve nucleotide-binding domains of these hexameric rings are coupled to protein disaggregation, highlighting similarities and differences between ClpB and Hsp104. (C) 2012 Elsevier Inc. All rights reserved.

引用

页码：161 / 171

页数：11

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